Characterization and functional properties of gelatin from goat bone through alcalase and neutrase enzymatic extraction

Abstract

Background and Aim: Gelatin is a dissolved protein that results from partial extraction of collagen, commonly from pig and bovine skin. There was no study on gelatin production from Kacang goat bones through enzymatic extraction. This study aimed to evaluate the chemical, physical, and functional properties of gelatin from bones of Kacang goat using alcalase and neutrase enzymes. Materials and Methods: Male Kacang goat bones aged 6-12 months and two commercial enzymes (alcalase and neutrase) were used for this study. Descriptive analysis and completely randomized design (one-way analysis of variance) were used to analyze the chemical, physical, and functional properties of gelatin. Kacang goat bone was extracted with four concentrations of alcalase and neutrase enzymes, namely, 0 U/g (AG-0 and NG-0), 0.02 U/g (AG-1 and NG-1), 0.04 U/g (AG-2 and NG-2), and 0.06 U/g (AG-3 and NG-3) with five replications. Results: The highest yield of gelatin extraction with alcalase obtained on AG-3 was 9.78%, and that with neutrase on NG-3 was 6.35%. The moisture content of alcalase gelatin was 9.39-9.94%, and that of neutrase gelatin was 9.15-9.24%. The ash and fat content of gelatin with alcalase was lower than that without enzyme treatment with higher protein content. The lowest fat content was noted in AG-1 (0.50%), with protein that was not different for all enzyme concentrations (69.65-70.21%). Gelatin with neutrase had lower ash content than that without neutrase (1.61-1.90%), with the highest protein content in NG-3 (70.89%). The pH of gelatin with alcalase and neutrase was 6.19-6.92 lower than that without enzymes. Melting points, gel strength, and water holding capacity (WHC) of gelatin with the highest alcalase levels on AG-1 and AG-2 ranged from 28.33 to 28.47°C, 67.41 to 68.14 g bloom, and 324.00 to 334.67%, respectively, with viscosity that did not differ, while the highest foam expansion (FE) and foam stability (FS) were noted in AG-1, which were 71.67% and 52.67%, respectively. The highest oil holding capacity (OHC) was found in AG-2 (283%). FS and OHC of gelatins with the highest neutrase levels in NG-2 were 30.00% and 265.33%, respectively, while gel strength, viscosity, FE, and WHC of gelatins with the highest neutrase levels did not differ with those without enzymes at all enzyme concentrations. B chain was degraded in all gelatins, and high-intensity a-chains in gelatin with alcalase and peptide fraction were formed in gelatin with neutrase. Extraction with enzymes showed loss of the triple helix as demonstrated by Fourier transform infrared spectroscopy. Conclusion: Based on the obtained results, the Kacang goat bone was the potential raw source for gelatin production. Enzymatic extraction can increase the quality of gelatin, especially the alcalase (0.02-0.04 U/g bone) method. This can be used to achieve the preferable quality of gelatin with a higher yield.

Conversion of waste animal bones to biofertilizer and adsorbent for wastewater treatment: An innovative approach to develop zero-waste technology

“…From the previous literature, it was shown that as compared to cow bone, higher concentration of TC, TN and other macro/micronutrients were recorded in the goat bone (Samoraj et ). It was also found that higher quantity of gelatin could be recorded in the bones of goat (Matulessy et al 2021). Therefore in the present study, the biofertilizer made from goat bone showed more plant growth as compared to that of biofertilizer made from cow.…”

Physicochemical Properties of Collagen from the Bone of Harpadon nehereus and Its Protective Effects against Angiotensin II-Induced Injury in Human Umbilical Vein Endothelial Cells

“…As shown in Figure , HNBC was rich in glycine (Gly, 253 residues), alanine (Ala, 124 residues), and proline (Pro, 99 residues), which was similar to amino acid compositions of many other bone collagens. ,,, Generally, Gly is the major amino acid and occurs as every third residue in collagen. The Gly content in HNBC was 253 residues/1000 residues, which was lower than those of many bone collagens (320–340 residues) but higher than that of channel catfish head bone gelatins (only more than 20%) and similar to Kacang goat bone gelatin . In addition, the content of glutamic acid (Glu) with 102 residues/1000 residues in HNBC was significantly higher than that in collagens from the carp bone (76 residues), black drum bone (68.7 residues), sheepshead bone (65.8 residues), deep-sea redfish bone, and leather jacket bone (35.8 residues) .…”

“…The Gly content in HNBC was 253 residues/1000 residues, which was lower than those of many bone collagens (320–340 residues) but higher than that of channel catfish head bone gelatins (only more than 20%) 42 and similar to Kacang goat bone gelatin. 43 In addition, the content of glutamic acid (Glu) with 102 residues/1000 residues in HNBC was significantly higher than that in collagens from the carp bone (76 residues), black drum bone (68.7 residues), 28 sheepshead bone (65.8 residues), 28 deep-sea redfish bone, 44 and leather jacket bone (35.8 residues). 29 Pro- and hydroxyproline (Hyp) were the unique amino acids in collagen, and their content is greatly related to the thermal stability of collagen.…”

A review on background, process and application of electrospun nanofibers for tissue regeneration

“…Gelatin is a protein obtained by the hydrolytic degradation of collagen from porcine or bovine origin. 58,59 It contains 18 different types of amino acids among which glycine, hydroxyproline and proline are the chief constituents of the total amino acid content. 60 For food industry, collagen is either boiled or enzymatically hydrolyzed to obtain colorless gelatin.…”